data_25108 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone Chemical Shift Assignment for the pfPP1 phosphatase regulator pfI2 of Plasmodium falciparum ; _BMRB_accession_number 25108 _BMRB_flat_file_name bmr25108.str _Entry_type original _Submission_date 2014-07-24 _Accession_date 2014-07-24 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'Backbone Chemical Shift Assignment for the pfPP1 phosphatase regulator pfI2 of Plasmodium falciparum' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Landrieu Isabelle . . 2 Cantrelle Francois-Xavier . . 3 Freville Aline . . 4 Khalife Jamal . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 95 "13C chemical shifts" 300 "15N chemical shifts" 93 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2014-08-26 original author . stop_ _Original_release_date 2014-08-26 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Identification of a Plasmodium falciparum inhibitor-2 motif involved in binding and regulation activity of the Protein Phosphatase type 1' _Citation_status 'in press' _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Freville Aline . . 2 Tellier Geraldine . . 3 Vandomme Audrey . . 4 Pierrot Christine . . 5 Vicogne Jerome . . 6 Cantrelle 'Fran ois-Xavier' . . 7 Martoriati Alain . . 8 Cailliau-Maggio Katia . . 9 Khalife Jamal . . 10 Landrieu Isabelle . . stop_ _Journal_abbreviation 'FEBS J.' _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year . _Details . loop_ _Keyword 'Plasmodium falciparum' 'protein phosphatase type 1' 'PP1 Inhibitor 2' 'NMR spectroscopy' 'protein-protein interaction' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name PfI2 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label PfI2 $PfI2 stop_ _System_molecular_weight 16701 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details Monomer save_ ######################## # Monomeric polymers # ######################## save_PfI2 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common PfI2 _Molecular_mass . _Mol_thiol_state 'all free' loop_ _Biological_function 'The regulation of PfPP1 phosphatase activity in Plasmodium falciparum' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 155 _Mol_residue_sequence ; RGSHHHHHHGSMKKKVDKSV TKKTISWDEVTINEQDKERG SRMKILEPNTPFNFILMDSA SEDEASKYGDVKGSDEGQNN IADDLINKLNQLVEKQENKG VSNIDFKEKRKKHYNEYKML QKLRKSGTLDDIDEEYKPDN KDSNCDNSNMNESEE ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -10 ARG 2 -9 GLY 3 -8 SER 4 -7 HIS 5 -6 HIS 6 -5 HIS 7 -4 HIS 8 -3 HIS 9 -2 HIS 10 -1 GLY 11 0 SER 12 1 MET 13 2 LYS 14 3 LYS 15 4 LYS 16 5 VAL 17 6 ASP 18 7 LYS 19 8 SER 20 9 VAL 21 10 THR 22 11 LYS 23 12 LYS 24 13 THR 25 14 ILE 26 15 SER 27 16 TRP 28 17 ASP 29 18 GLU 30 19 VAL 31 20 THR 32 21 ILE 33 22 ASN 34 23 GLU 35 24 GLN 36 25 ASP 37 26 LYS 38 27 GLU 39 28 ARG 40 29 GLY 41 30 SER 42 31 ARG 43 32 MET 44 33 LYS 45 34 ILE 46 35 LEU 47 36 GLU 48 37 PRO 49 38 ASN 50 39 THR 51 40 PRO 52 41 PHE 53 42 ASN 54 43 PHE 55 44 ILE 56 45 LEU 57 46 MET 58 47 ASP 59 48 SER 60 49 ALA 61 50 SER 62 51 GLU 63 52 ASP 64 53 GLU 65 54 ALA 66 55 SER 67 56 LYS 68 57 TYR 69 58 GLY 70 59 ASP 71 60 VAL 72 61 LYS 73 62 GLY 74 63 SER 75 64 ASP 76 65 GLU 77 66 GLY 78 67 GLN 79 68 ASN 80 69 ASN 81 70 ILE 82 71 ALA 83 72 ASP 84 73 ASP 85 74 LEU 86 75 ILE 87 76 ASN 88 77 LYS 89 78 LEU 90 79 ASN 91 80 GLN 92 81 LEU 93 82 VAL 94 83 GLU 95 84 LYS 96 85 GLN 97 86 GLU 98 87 ASN 99 88 LYS 100 89 GLY 101 90 VAL 102 91 SER 103 92 ASN 104 93 ILE 105 94 ASP 106 95 PHE 107 96 LYS 108 97 GLU 109 98 LYS 110 99 ARG 111 100 LYS 112 101 LYS 113 102 HIS 114 103 TYR 115 104 ASN 116 105 GLU 117 106 TYR 118 107 LYS 119 108 MET 120 109 LEU 121 110 GLN 122 111 LYS 123 112 LEU 124 113 ARG 125 114 LYS 126 115 SER 127 116 GLY 128 117 THR 129 118 LEU 130 119 ASP 131 120 ASP 132 121 ILE 133 122 ASP 134 123 GLU 135 124 GLU 136 125 TYR 137 126 LYS 138 127 PRO 139 128 ASP 140 129 ASN 141 130 LYS 142 131 ASP 143 132 SER 144 133 ASN 145 134 CYS 146 135 ASP 147 136 ASN 148 137 SER 149 138 ASN 150 139 MET 151 140 ASN 152 141 GLU 153 142 SER 154 143 GLU 155 144 GLU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-08-05 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value EMBL CAX64439 "conserved Plasmodium protein, unknown function [Plasmodium falciparum 3D7]" 92.90 144 100.00 100.00 2.66e-97 EMBL CDO62624 "protein phosphatase inhibitor 2, putative [Plasmodium reichenowi]" 92.90 144 98.61 100.00 3.31e-96 GB ETW20523 "hypothetical protein PFFVO_00575 [Plasmodium falciparum Vietnam Oak-Knoll (FVO)]" 92.90 144 100.00 100.00 2.66e-97 GB ETW38648 "hypothetical protein PFTANZ_00648 [Plasmodium falciparum Tanzania (2000708)]" 86.45 142 100.00 100.00 4.83e-90 GB ETW45017 "hypothetical protein PFNF135_00618 [Plasmodium falciparum NF135/5.C10]" 92.90 144 100.00 100.00 2.66e-97 GB ETW51416 "hypothetical protein PFMALIP_00574 [Plasmodium falciparum MaliPS096_E11]" 92.90 144 100.00 100.00 2.66e-97 GB ETW52113 "hypothetical protein PFUGPA_05729 [Plasmodium falciparum Palo Alto/Uganda]" 92.90 144 100.00 100.00 2.66e-97 REF XP_002808630 "conserved Plasmodium protein, unknown function [Plasmodium falciparum 3D7]" 92.90 144 100.00 100.00 2.66e-97 REF XP_012761271 "protein phosphatase inhibitor 2, putative [Plasmodium reichenowi]" 92.90 144 98.61 100.00 3.31e-96 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Gene_mnemonic _Details $PfI2 'malaria parasite P. falciparum' 5833 Eukaryota . Plasmodium falciparum Pf3D7 'Protein phosphatase inhibitor 2' stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $PfI2 'recombinant technology' . Escherichia coli M15 pQE30 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $PfI2 . mM 0.05 0.1 '[U-98% 15N]' 'sodium phosphate' 100 mM . . 'natural abundance' 'sodium chloride' 100 mM . . 'natural abundance' EDTA 2.5 mM . . 'natural abundance' DTT 10 mM . . 'natural abundance' TSP 0.1 mM . . 'natural abundance' D2O 5 % . . 'natural abundance' H2O 95 % . . 'natural abundance' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $PfI2 . mM 0.05 0.2 '[U-98% 13C; U-98% 15N]' 'sodium phosphate' 100 mM . . 'natural abundance' 'sodium chloride' 100 mM . . 'natural abundance' EDTA 2.5 mM . . 'natural abundance' DTT 10 mM . . 'natural abundance' TSP 0.1 mM . . 'natural abundance' D2O 5 % . . 'natural abundance' H2O 95 % . . 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'peak picking' stop_ _Details . save_ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version 2.1 loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task processing stop_ _Details . save_ save_Mars _Saveframe_category software _Name Mars _Version . loop_ _Vendor _Address _Electronic_address 'Jung YS & Zweckstetter M' . http://www3.mpibpc.mpg.de/groups/zweckstetter/_links/software_mars.htm stop_ loop_ _Task 'chemical shift assignment' stop_ _Details 'Jung YS & Zweckstetter M (2004) Mars -- robust automatic backbone assignment of proteins, J Biomol NMR. 30, 11-23.' save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 600 _Details Cryoprobe save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_2 save_ save_3D_HNCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_2 save_ save_3D_CBCA(CO)NH_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_2 save_ save_3D_HNCO_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_2 save_ save_3D_HN(CA)CO_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _Sample_label $sample_2 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units temperature 298 . K pH 6.7 . pH pressure 1 . atm 'ionic strength' 100 . mM stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio TSP H 1 'methyl protons' ppm 0 internal direct . . . 1.0 TSP C 13 'methyl protons' ppm 0 internal indirect . . . 0.101329118 TSP N 15 'methyl protons' ppm 0 internal indirect . . . 0.251449530 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCACB' '3D HNCA' '3D HNCO' '3D CBCA(CO)NH' '3D HN(CA)CO' stop_ loop_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name PfI2 _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 3 14 LYS H H 8.37 . 1 2 3 14 LYS C C 176.4 . 1 3 3 14 LYS CA C 56.44 . 1 4 3 14 LYS CB C 33.06 . 1 5 3 14 LYS N N 123.8 . 1 6 4 15 LYS H H 8.28 . 1 7 4 15 LYS C C 176.3 . 1 8 4 15 LYS CA C 56.44 . 1 9 4 15 LYS CB C 33.19 . 1 10 4 15 LYS N N 123 . 1 11 5 16 VAL H H 8.23 . 1 12 5 16 VAL C C 175.6 . 1 13 5 16 VAL CA C 62.13 . 1 14 5 16 VAL CB C 33.02 . 1 15 5 16 VAL N N 122.3 . 1 16 6 17 ASP H H 8.43 . 1 17 6 17 ASP C C 176.3 . 1 18 6 17 ASP CA C 54.18 . 1 19 6 17 ASP CB C 41.62 . 1 20 6 17 ASP N N 125.2 . 1 21 7 18 LYS H H 8.42 . 1 22 7 18 LYS C C 176.7 . 1 23 7 18 LYS CA C 56.53 . 1 24 7 18 LYS CB C 32.68 . 1 25 7 18 LYS N N 122.9 . 1 26 8 19 SER H H 8.45 . 1 27 8 19 SER C C 174.7 . 1 28 8 19 SER CA C 59.02 . 1 29 8 19 SER CB C 63.87 . 1 30 8 19 SER N N 117.1 . 1 31 9 20 VAL H H 8.05 . 1 32 9 20 VAL C C 176.4 . 1 33 9 20 VAL CA C 62.49 . 1 34 9 20 VAL CB C 32.53 . 1 35 9 20 VAL N N 121.4 . 1 36 10 21 THR H H 8.17 . 1 37 10 21 THR C C 174.4 . 1 38 10 21 THR CA C 62.15 . 1 39 10 21 THR CB C 69.71 . 1 40 10 21 THR N N 118.2 . 1 41 11 22 LYS H H 8.30 . 1 42 11 22 LYS C C 176.3 . 1 43 11 22 LYS CA C 56.42 . 1 44 11 22 LYS CB C 33.29 . 1 45 11 22 LYS N N 124.4 . 1 46 12 23 LYS H H 8.36 . 1 47 12 23 LYS C C 176.5 . 1 48 12 23 LYS CA C 56.45 . 1 49 12 23 LYS CB C 33.19 . 1 50 12 23 LYS N N 123.2 . 1 51 13 24 THR H H 8.20 . 1 52 13 24 THR C C 174.2 . 1 53 13 24 THR CA C 62.15 . 1 54 13 24 THR CB C 69.64 . 1 55 13 24 THR N N 116.8 . 1 56 14 25 ILE H H 8.18 . 1 57 14 25 ILE C C 175.7 . 1 58 14 25 ILE CA C 61.05 . 1 59 14 25 ILE CB C 69.64 . 1 60 14 25 ILE N N 123.5 . 1 61 15 26 SER H H 8.24 . 1 62 15 26 SER C C 174.4 . 1 63 15 26 SER CA C 57.85 . 1 64 15 26 SER CB C 63.93 . 1 65 15 26 SER N N 120.0 . 1 66 16 27 TRP H H 8.22 . 1 67 16 27 TRP C C 175.9 . 1 68 16 27 TRP CA C 57.75 . 1 69 16 27 TRP CB C 29.60 . 1 70 16 27 TRP N N 123.8 . 1 71 17 28 ASP H H 8.15 . 1 72 17 28 ASP C C 176 . 1 73 17 28 ASP CA C 54.44 . 1 74 17 28 ASP CB C 40.92 . 1 75 17 28 ASP N N 120.7 . 1 76 18 29 GLU H H 8.04 . 1 77 18 29 GLU C C 176.6 . 1 78 18 29 GLU CA C 56.96 . 1 79 18 29 GLU CB C 30.3 . 1 80 18 29 GLU N N 120.5 . 1 81 19 30 VAL H H 8.05 . 1 82 19 30 VAL C C 176.6 . 1 83 19 30 VAL CA C 62.97 . 1 84 19 30 VAL CB C 32.58 . 1 85 19 30 VAL N N 120.8 . 1 86 20 31 THR H H 8.21 . 1 87 20 31 THR C C 174.7 . 1 88 20 31 THR CA C 62.41 . 1 89 20 31 THR CB C 69.58 . 1 90 20 31 THR N N 118.4 . 1 91 21 32 ILE H H 8.12 . 1 92 21 32 ILE C C 176 . 1 93 21 32 ILE CA C 61.48 . 1 94 21 32 ILE CB C 38.72 . 1 95 21 32 ILE N N 123.4 . 1 96 22 33 ASN H H 8.49 . 1 97 22 33 ASN C C 175.7 . 1 98 22 33 ASN CA C 53.53 . 1 99 22 33 ASN CB C 38.92 . 1 100 22 33 ASN N N 123.4 . 1 101 23 34 GLU H H 8.48 . 1 102 23 34 GLU C C 177.2 . 1 103 23 34 GLU CA C 57.68 . 1 104 23 34 GLU CB C 30.03 . 1 105 23 34 GLU N N 121.9 . 1 106 24 35 GLN H H 8.34 . 1 107 24 35 GLN C C 176.5 . 1 108 24 35 GLN CA C 56.94 . 1 109 24 35 GLN CB C 29.08 . 1 110 24 35 GLN N N 119.7 . 1 111 25 36 ASP H H 8.23 . 1 112 25 36 ASP C C 177 . 1 113 25 36 ASP CA C 55.02 . 1 114 25 36 ASP CB C 40.95 . 1 115 25 36 ASP N N 120.6 . 1 116 26 37 LYS H H 8.11 . 1 117 26 37 LYS C C 177.4 . 1 118 26 37 LYS CA C 57.46 . 1 119 26 37 LYS CB C 32.81 . 1 120 26 37 LYS N N 121.5 . 1 121 27 38 GLU H H 8.29 . 1 122 27 38 GLU C C 177.2 . 1 123 27 38 GLU CA C 57.21 . 1 124 27 38 GLU CB C 29.72 . 1 125 27 38 GLU N N 120.3 . 1 126 28 39 ARG H H 8.287 . 1 127 28 39 ARG C C 177.3 . 1 128 28 39 ARG CA C 56.53 . 1 129 28 39 ARG CB C 30.52 . 1 130 28 39 ARG N N 121.1 . 1 131 29 40 GLY H H 8.38 . 1 132 29 40 GLY C C 174.7 . 1 133 29 40 GLY CA C 45.7 . 1 134 29 40 GLY N N 109 . 1 135 30 41 SER H H 8.17 . 1 136 30 41 SER C C 175.1 . 1 137 30 41 SER CA C 58.83 . 1 138 30 41 SER CB C 63.79 . 1 139 30 41 SER N N 115.6 . 1 140 31 42 ARG H H 8.29 . 1 141 31 42 ARG C C 176.4 . 1 142 31 42 ARG CA C 56.53 . 1 143 31 42 ARG CB C 30.52 . 1 144 31 42 ARG N N 122.4 . 1 145 32 43 MET CA C 55.7 . 1 146 32 43 MET CB C 32.81 . 1 147 33 44 LYS H H 8.24 . 1 148 33 44 LYS C C 176.1 . 1 149 33 44 LYS CA C 56.44 . 1 150 33 44 LYS CB C 32.95 . 1 151 33 44 LYS N N 122.7 . 1 152 34 45 ILE H H 8.12 . 1 153 34 45 ILE CA C 61.17 . 1 154 34 45 ILE CB C 38.7 . 1 155 34 45 ILE N N 122.6 . 1 156 35 46 LEU H H 8.24 . 1 157 35 46 LEU CA C 55.1 . 1 158 35 46 LEU CB C 42.44 . 1 159 35 46 LEU N N 126.5 . 1 160 37 48 PRO CA C 63.49 . 1 161 37 48 PRO CB C 32.17 . 1 162 38 49 ASN H H 8.56 . 1 163 38 49 ASN CA C 53.48 . 1 164 38 49 ASN CB C 38.54 . 1 165 38 49 ASN N N 118.1 . 1 166 39 50 THR H H 7.97 . 1 167 39 50 THR C C 174.4 . 1 168 39 50 THR CA C 59.91 . 1 169 39 50 THR CB C 69.82 . 1 170 39 50 THR N N 116.3 . 1 171 40 51 PRO C C 176.6 . 1 172 40 51 PRO CA C 63.38 . 1 173 40 51 PRO CB C 31.97 . 1 174 41 52 PHE H H 8.15 . 1 175 41 52 PHE C C 174.7 . 1 176 41 52 PHE CA C 57.96 . 1 177 41 52 PHE CB C 39.49 . 1 178 41 52 PHE N N 120 . 1 179 42 53 ASN CA C 52.99 . 1 180 42 53 ASN CB C 38.75 . 1 181 43 54 PHE H H 7.95 . 1 182 43 54 PHE C C 175.1 . 1 183 43 54 PHE CA C 58.15 . 1 184 43 54 PHE CB C 39.73 . 1 185 43 54 PHE N N 120.6 . 1 186 44 55 ILE H H 8.06 . 1 187 44 55 ILE CA C 60.91 . 1 188 45 56 LEU CA C 55.49 . 1 189 45 56 LEU CB C 41.25 . 1 190 46 57 MET H H 8.33 . 1 191 46 57 MET C C 176.4 . 1 192 46 57 MET CA C 56.77 . 1 193 46 57 MET CB C 32.69 . 1 194 46 57 MET N N 121.7 . 1 195 47 58 ASP H H 8.33 . 1 196 47 58 ASP C C 176.4 . 1 197 47 58 ASP CA C 54.72 . 1 198 47 58 ASP CB C 41.4 . 1 199 47 58 ASP N N 121.7 . 1 200 48 59 SER H H 8.25 . 1 201 48 59 SER C C 174.5 . 1 202 48 59 SER CA C 58.7 . 1 203 48 59 SER CB C 64 . 1 204 48 59 SER N N 116.3 . 1 205 49 60 ALA H H 8.32 . 1 206 49 60 ALA C C 178 . 1 207 49 60 ALA CA C 52.84 . 1 208 49 60 ALA CB C 19.22 . 1 209 49 60 ALA N N 125.8 . 1 210 50 61 SER H H 8.23 . 1 211 50 61 SER CA C 58.72 . 1 212 50 61 SER CB C 63.92 . 1 213 50 61 SER N N 115.1 . 1 214 51 62 GLU H H 8.46 . 1 215 51 62 GLU CA C 57.08 . 1 216 51 62 GLU CB C 30.17 . 1 217 51 62 GLU N N 122.8 . 1 218 52 63 ASP H H 8.30 . 1 219 52 63 ASP CA C 54.74 . 1 220 52 63 ASP CB C 41.29 . 1 221 52 63 ASP N N 121 . 1 222 53 64 GLU H H 8.33 . 1 223 53 64 GLU C C 177.1 . 1 224 53 64 GLU CA C 57.73 . 1 225 53 64 GLU CB C 30.07 . 1 226 53 64 GLU N N 121.9 . 1 227 54 65 ALA H H 8.25 . 1 228 54 65 ALA C C 178.8 . 1 229 54 65 ALA CA C 53.59 . 1 230 54 65 ALA CB C 18.86 . 1 231 54 65 ALA N N 123.1 . 1 232 55 66 SER H H 8.08 . 1 233 55 66 SER C C 175.1 . 1 234 55 66 SER CA C 59.12 . 1 235 55 66 SER CB C 63.54 . 1 236 55 66 SER N N 113.9 . 1 237 56 67 LYS H H 7.96 . 1 238 56 67 LYS C C 176.6 . 1 239 56 67 LYS CA C 57.03 . 1 240 56 67 LYS CB C 32.84 . 1 241 56 67 LYS N N 122.4 . 1 242 57 68 TYR H H 7.99 . 1 243 57 68 TYR C C 176.4 . 1 244 57 68 TYR CA C 57.94 . 1 245 57 68 TYR CB C 38.62 . 1 246 57 68 TYR N N 119.4 . 1 247 58 69 GLY H H 8.12 . 1 248 58 69 GLY C C 173.6 . 1 249 58 69 GLY CA C 45.39 . 1 250 58 69 GLY N N 109.7 . 1 251 59 70 ASP H H 8.2 . 1 252 59 70 ASP C C 176.4 . 1 253 59 70 ASP CA C 54.33 . 1 254 59 70 ASP CB C 41.31 . 1 255 59 70 ASP N N 120.7 . 1 256 60 71 VAL H H 8.1 . 1 257 60 71 VAL C C 176.3 . 1 258 60 71 VAL CA C 62.45 . 1 259 60 71 VAL CB C 32.67 . 1 260 60 71 VAL N N 120.5 . 1 261 61 72 LYS H H 8.43 . 1 262 61 72 LYS C C 177.1 . 1 263 61 72 LYS CA C 56.47 . 1 264 61 72 LYS CB C 32.87 . 1 265 61 72 LYS N N 125.4 . 1 266 62 73 GLY H H 8.45 . 1 267 62 73 GLY C C 174.3 . 1 268 62 73 GLY CA C 45.31 . 1 269 62 73 GLY N N 110.5 . 1 270 63 74 SER H H 8.27 . 1 271 63 74 SER C C 174.5 . 1 272 63 74 SER CA C 58.51 . 1 273 63 74 SER CB C 64.07 . 1 274 63 74 SER N N 115.6 . 1 275 64 75 ASP H H 8.47 . 1 276 64 75 ASP C C 176.5 . 1 277 64 75 ASP CA C 54.54 . 1 278 64 75 ASP CB C 41.21 . 1 279 64 75 ASP N N 122.4 . 1 280 65 76 GLU H H 8.37 . 1 281 65 76 GLU C C 177.3 . 1 282 65 76 GLU CA C 57.17 . 1 283 65 76 GLU CB C 30.03 . 1 284 65 76 GLU N N 121.3 . 1 285 66 77 GLY H H 8.47 . 1 286 66 77 GLY C C 174.5 . 1 287 66 77 GLY CA C 45.64 . 1 288 66 77 GLY N N 109.6 . 1 289 67 78 GLN H H 8.18 . 1 290 67 78 GLN C C 175.9 . 1 291 67 78 GLN CA C 55.98 . 1 292 67 78 GLN CB C 29.29 . 1 293 67 78 GLN N N 119.4 . 1 294 68 79 ASN H H 8.46 . 1 295 68 79 ASN C C 174.9 . 1 296 68 79 ASN CA C 53.4 . 1 297 68 79 ASN CB C 38.9 . 1 298 68 79 ASN N N 119.4 . 1 299 69 80 ASN H H 8.40 . 1 300 69 80 ASN C C 175.2 . 1 301 69 80 ASN CA C 53.44 . 1 302 69 80 ASN CB C 38.84 . 1 303 69 80 ASN N N 119.4 . 1 304 70 81 ILE H H 8.08 . 1 305 70 81 ILE C C 176.2 . 1 306 70 81 ILE CA C 61.5 . 1 307 70 81 ILE CB C 38.8 . 1 308 70 81 ILE N N 121.3 . 1 309 71 82 ALA H H 8.31 . 1 310 71 82 ALA C C 177.9 . 1 311 71 82 ALA CA C 52.96 . 1 312 71 82 ALA CB C 19.26 . 1 313 71 82 ALA N N 127.4 . 1 314 72 83 ASP H H 8.18 . 1 315 72 83 ASP C C 176.6 . 1 316 72 83 ASP CA C 55.22 . 1 317 72 83 ASP CB C 41.14 . 1 318 72 83 ASP N N 119.7 . 1 319 73 84 ASP H H 8.24 . 1 320 73 84 ASP C C 177.1 . 1 321 73 84 ASP CA C 55.31 . 1 322 73 84 ASP CB C 40.92 . 1 323 73 84 ASP N N 120 . 1 324 74 85 LEU H H 8.03 . 1 325 74 85 LEU CA C 56.55 . 1 326 74 85 LEU CB C 41.94 . 1 327 75 86 ILE H H 7.85 . 1 328 75 86 ILE CA C 62.56 . 1 329 75 86 ILE CB C 38.09 . 1 330 75 86 ILE N N 119.5 . 1 331 79 90 ASN C C 175.7 . 1 332 79 90 ASN CA C 53.81 . 1 333 79 90 ASN CB C 38.54 . 1 334 80 91 GLN H H 8.09 . 1 335 80 91 GLN C C 176.2 . 1 336 80 91 GLN CA C 56.55 . 1 337 80 91 GLN CB C 29.1 . 1 338 80 91 GLN N N 119.5 . 1 339 85 96 GLN C C 176.2 . 1 340 85 96 GLN CA C 56.04 . 1 341 85 96 GLN CB C 29.29 . 1 342 86 97 GLU H H 8.54 . 1 343 86 97 GLU C C 176.2 . 1 344 86 97 GLU CA C 56.85 . 1 345 86 97 GLU CB C 30.29 . 1 346 86 97 GLU N N 122.1 . 1 347 89 100 GLY C C 174.2 . 1 348 89 100 GLY CA C 45.44 . 1 349 90 101 VAL H H 7.96 . 1 350 90 101 VAL C C 176.3 . 1 351 90 101 VAL CA C 62.31 . 1 352 90 101 VAL CB C 32.88 . 1 353 90 101 VAL N N 118.9 . 1 354 91 102 SER H H 8.43 . 1 355 91 102 SER CA C 58.34 . 1 356 91 102 SER CB C 63.96 . 1 357 91 102 SER N N 119.2 . 1 358 92 103 ASN C C 175.3 . 1 359 92 103 ASN CA C 53.61 . 1 360 92 103 ASN CB C 38.89 . 1 361 93 104 ILE H H 8.01 . 1 362 93 104 ILE C C 175.7 . 1 363 93 104 ILE CA C 61.62 . 1 364 93 104 ILE CB C 38.8 . 1 365 93 104 ILE N N 120.5 . 1 366 94 105 ASP H H 8.25 . 1 367 94 105 ASP C C 176.5 . 1 368 94 105 ASP CA C 54.42 . 1 369 94 105 ASP CB C 41.25 . 1 370 94 105 ASP N N 123.7 . 1 371 116 127 GLY C C 174.3 . 1 372 116 127 GLY CA C 45.52 . 1 373 117 128 THR H H 8.05 . 1 374 117 128 THR C C 174.4 . 1 375 117 128 THR CA C 61.82 . 1 376 117 128 THR CB C 69.96 . 1 377 117 128 THR N N 113.4 . 1 378 118 129 LEU H H 8.33 . 1 379 118 129 LEU CA C 55.35 . 1 380 118 129 LEU CB C 42.23 . 1 381 118 129 LEU N N 123.5 . 1 382 119 130 ASP CA C 54.6 . 1 383 119 130 ASP CB C 41.4 . 1 384 120 131 ASP H H 8.18 . 1 385 120 131 ASP C C 176.1 . 1 386 120 131 ASP CA C 54.5 . 1 387 120 131 ASP CB C 41.2 . 1 388 120 131 ASP N N 120.1 . 1 389 121 132 ILE H H 7.97 . 1 390 121 132 ILE C C 175.9 . 1 391 121 132 ILE CA C 61.27 . 1 392 121 132 ILE CB C 39.01 . 1 393 121 132 ILE N N 120.1 . 1 394 122 133 ASP H H 8.35 . 1 395 122 133 ASP C C 176.5 . 1 396 122 133 ASP CA C 54.49 . 1 397 122 133 ASP CB C 41.42 . 1 398 122 133 ASP N N 124.2 . 1 399 123 134 GLU H H 8.31 . 1 400 123 134 GLU CA C 56.87 . 1 401 123 134 GLU CB C 30.51 . 1 402 124 135 GLU N N 121.7 . 1 403 125 136 TYR H H 8.20 . 1 404 125 136 TYR C C 175.1 . 1 405 125 136 TYR CA C 58.06 . 1 406 125 136 TYR CB C 38.58 . 1 407 125 136 TYR N N 122.2 . 1 408 126 137 LYS H H 8.00 . 1 409 126 137 LYS C C 173.7 . 1 410 126 137 LYS CA C 53.59 . 1 411 126 137 LYS CB C 32.94 . 1 412 126 137 LYS N N 126.4 . 1 413 127 138 PRO C C 176.6 . 1 414 127 138 PRO CA C 63.14 . 1 415 127 138 PRO CB C 32.05 . 1 416 128 139 ASP H H 8.36 . 1 417 128 139 ASP C C 176.1 . 1 418 128 139 ASP CA C 54.28 . 1 419 128 139 ASP CB C 41.18 . 1 420 128 139 ASP N N 120.1 . 1 421 129 140 ASN H H 8.29 . 1 422 129 140 ASN C C 175.4 . 1 423 129 140 ASN CA C 53.36 . 1 424 129 140 ASN CB C 38.86 . 1 425 129 140 ASN N N 119.4 . 1 426 132 143 SER H H 8.21 . 1 427 132 143 SER C C 174.5 . 1 428 132 143 SER CA C 58.84 . 1 429 132 143 SER CB C 63.8 . 1 430 132 143 SER N N 116.2 . 1 431 133 144 ASN H H 8.49 . 1 432 133 144 ASN C C 175.3 . 1 433 133 144 ASN CA C 53.56 . 1 434 133 144 ASN CB C 38.85 . 1 435 133 144 ASN N N 120.7 . 1 436 134 145 CYS H H 8.23 . 1 437 134 145 CYS C C 174.2 . 1 438 134 145 CYS CA C 58.68 . 1 439 134 145 CYS CB C 28.13 . 1 440 134 145 CYS N N 119.1 . 1 441 135 146 ASP H H 8.41 . 1 442 135 146 ASP C C 176.1 . 1 443 135 146 ASP CA C 54.46 . 1 444 135 146 ASP CB C 41.17 . 1 445 135 146 ASP N N 122.7 . 1 446 136 147 ASN H H 8.37 . 1 447 136 147 ASN C C 175.6 . 1 448 136 147 ASN CA C 53.41 . 1 449 136 147 ASN CB C 38.94 . 1 450 136 147 ASN N N 119.9 . 1 451 137 148 SER H H 8.35 . 1 452 137 148 SER C C 174.5 . 1 453 137 148 SER CA C 59.29 . 1 454 137 148 SER CB C 63.73 . 1 455 137 148 SER N N 116.3 . 1 456 138 149 ASN H H 8.43 . 1 457 138 149 ASN C C 175.3 . 1 458 138 149 ASN CA C 53.47 . 1 459 138 149 ASN CB C 38.67 . 1 460 138 149 ASN N N 120.2 . 1 461 139 150 MET C C 176 . 1 462 139 150 MET CA C 57.02 . 1 463 139 150 MET CB C 32.72 . 1 464 140 151 ASN H H 8.43 . 1 465 140 151 ASN C C 175.2 . 1 466 140 151 ASN CA C 53.58 . 1 467 140 151 ASN CB C 38.99 . 1 468 140 151 ASN N N 119.6 . 1 469 141 152 GLU H H 8.41 . 1 470 141 152 GLU C C 176.5 . 1 471 141 152 GLU CA C 56.73 . 1 472 141 152 GLU CB C 30.36 . 1 473 141 152 GLU N N 121.5 . 1 474 142 153 SER H H 8.31 . 1 475 142 153 SER C C 174.4 . 1 476 142 153 SER CA C 58.46 . 1 477 142 153 SER CB C 64.09 . 1 478 142 153 SER N N 116.4 . 1 479 143 154 GLU H H 8.43 . 1 480 143 154 GLU C C 175.6 . 1 481 143 154 GLU CA C 56.62 . 1 482 143 154 GLU CB C 30.54 . 1 483 143 154 GLU N N 123.4 . 1 484 144 155 GLU H H 7.99 . 1 485 144 155 GLU CA C 58.21 . 1 486 144 155 GLU CB C 31.09 . 1 487 144 155 GLU CG C 181.2 . 1 488 144 155 GLU N N 126.7 . 1 stop_ save_